A designed heme-[4Fe-4S] metalloenzyme catalyzes sulfite reduction like the native enzyme

De novo design of a hyperstable non-natural protein–ligand complex with sub-Å accuracy

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A bioinspired iron catalyst for nitrate and perchlorate reduction

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A Designed Metalloenzyme Achieving the Catalytic Rate of a Native Enzyme

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O-S Bond Activation in Structures Isoelectronic with Ferric Peroxide Species Known in O-O-Activating Enzymes: Relevance for Sulfide Activation and Sulfite Reductases

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Mutational Analysis of Sulfite Reductase Hemoprotein Reveals the Mechanism for Coordinated Electron and Proton Transfer

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Biotinylated Rh(III) Complexes in Engineered Streptavidin for Accelerated Asymmetric C-H Activation

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[Fe4S4]- and [Fe3S4]-cluster formation in synthetic peptides

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Hydrolytic catalysis and structural stabilization in a designed metalloprotein

(2011) Melissa L. Zastrow et al.   Nature Chemistry

MarkUs: a server to navigate sequence-structure-function space

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Spectroscopic features of cytochrome P450 reaction intermediates

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Computational Design of an Enzyme Catalyst for a Stereoselective Bimolecular Diels-Alder Reaction

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VASP: A Volumetric Analysis of Surface Properties Yields Insights into Protein-Ligand Binding Specificity

(2010) Brian Y. Chen et al.   PLoS Computational Biology

Comparison of Cyanide and Carbon Monoxide as Ligands in Iron(II) Porphyrinates

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Density Functional Theory Calculation of Bonding and Charge Parameters for Molecular Dynamics Studies on [FeFe] Hydrogenases

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